生物
甲基化
甲基转移酶
核酸
蛋白质精氨酸甲基转移酶5
精氨酸
核糖核酸
生物化学
蛋白质甲基化
RNA结合蛋白
细胞生物学
基因
氨基酸
作者
Jonathan D. Gary,Steven Clarke
出处
期刊:Progress in Nucleic Acid Research and Molecular Biology
日期:1998-01-01
卷期号:: 65-131
被引量:479
标识
DOI:10.1016/s0079-6603(08)60825-9
摘要
This review summarizes the current status of protein arginine N-methylation reactions. These covalent modifications of proteins are now recognized in a number of eukaryotic proteins and their functional significance is beginning to be understood. Genes that encode those methyltransferases specific for catalyzing the formation of asymmetric dimethylarginine have been identified. The enzyme modifies a number of generally nuclear or nucleolar proteins that interact with nucleic acids, particularly RNA. Postulated roles for these reactions include signal transduction, nuclear transport, or a direct modulation of nucleic acid interactions. A second methyltransferase activity that symmetrically dimethylates an arginine residue in myelin basic protein, a major component of the axon sheath, has also been characterized. However, a gene encoding this activity has not been identified to date and the cellular function for this methylation reaction has not been clearly established. From the analysis of the sequences surrounding known arginine methylation sites, we have determined consensus methyl-accepting sequences that may be useful in identifying novel substrates for these enzymes and may shed further light on their physiological role.
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